Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0021345 (infectious mononucleosis)
 3,358 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The major sialoglycopeptide released from bovine erythrocytes by papain has been purified and characterized. The glycopeptide contains 82% by weight carbohydrate in molar ratios of galactose - 5.5:N-acetylglucosamine - 3.6:sialic acid - 2.6:N-acetylgalactosamine - 1.0. The carbohydrate and amino acid composition is quite different from the glycoprotein extracted from bovine erythrocyte stroma with hot 75% ethanol. The glycopeptide is devoid of reactivity with Paul-Bunnell heterophile antibody of infectious mononucleosis - an activity expressed to high degree on the bovine erythrocyte and associated with glycoprotein. The glycopeptide does react, however, with another antibody found in infectious mononucleosis as well as most normal human sera tested.
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PMID:Immunochemical studies of infectious mononucleosis. VII. Isolation and partial characterization of a glycopeptide from bovine erythrocytes. 89 34

A glycoprotein was isolated from the membrane of the bovine erythrocyte by refluxing the acetone- and ethanol-extracted stroma residue with 75% ethanol. The glycoprotein was purified by phosphocellulose chromatography, ethanol precipitation, lipidsolvent extraction and DEAE chromatography. The glycoprotein appeared to have two serological determinants, both reactive with antibodies present in the sera of patients with infectious mononucleosis. One of the determinants is similar to the Paul-Bunnell heterophile antigen found on sheep erythrocytes. It is dependent on carbohydrate, including sialic acid residues. Another specificity, seemingly not shared by sheep erythrocytes to any great extent, is resistance to neuraminidase and to alkaline borohydride treatment and thus it may be located either on the polypeptide portion of the molecule or on an alkali-stable oligosaccharide. The purified glycoprotein comprises 73% amino acids. Carbohydrate components and their molar ratios were sialic acid (1.0): galactose (1.5): N-acetylglucosamine (1.1): N-acetylgalactosamine (0.5): mannose (0.1).
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PMID:Immunochemical studies of infectious mononucleosis. IX. Heterophile antigen associated with a glycoprotein from the bovine erythrocyte membrane. 681 86

A glycoprotein was solubilized from sheep erythrocyte membranes with hot aqueous ethanol. The glycoprotein was purified by phosphocellulose chromatography, ethanol precipitation, lipid solvent extraction, and DEAE chromatography. In water solution the glycoprotein existed as globular aggregates with a diameter of 7.1 +/- 2.2 nm. In the presence of sodium dodecyl sulfate, 80% of the material exhibited a subunit m.w.app of 27,000. Approximately 10% of the material had a m.w.app of only 9000 and another 10% had a m.w.app of 35,000. All three fractions were reactive with Paul-Bunnell heterophile antibody from the sera of patients with infectious mononucleosis and with Limulus polyphemus lectin. These activities were destroyed by neuraminidase treatment. Complete inhibition of the rosetting of sheep red blood cells by 4 X 10(5) human peripheral blood lymphocytes was seen at 100 to 200 micrograms glycoprotein/ml. Neuraminidase-treated glycoprotein was not inhibitory. Pronase-derived sialoglycopeptide was inhibitory. Most likely, the receptor for lymphocytes resides in the carbohydrate portion of the glycoprotein. By using 125I-glycoprotein, binding studies were carried out that yielded an estimate of approximately 2 X 10(5) binding sites for sheep erythrocyte glycoprotein per lymphocyte. Purified glycoprotein contained 44.4% amino acid. Carbohydrate components and their molar ratios were sialic acid (1.0): galactose (1.0):N-acetylglucosamine (1.3): N-acetylgalactosamine (1.2).
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PMID:Immunochemical studies of infectious mononucleosis. VIII. A glycoprotein from sheep erythrocytes with sialic acid-dependent receptor properties. 705 98